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P70377 (FGF13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor 13

Short name=FGF-13
Alternative name(s):
Fibroblast growth factor homologous factor 2
Short name=FHF-2
Gene names
Name:Fgf13
Synonyms:Fhf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, may participate to the refinement of axons by negatively regulating axonal and leading processes branching. Plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus. Ref.8 Ref.9 Ref.10 Ref.11

Isoform 1 seems not to be involved in neuroblast polarization and migration but regulates axon branching. Ref.8 Ref.9 Ref.10 Ref.11

May regulate voltage-gated sodium channels transport and function. Ref.8 Ref.9 Ref.10 Ref.11

May also play a role in MAPK signaling. Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Interacts with SCN8A; may regulate SCN8A activity By similarity. Interacts with SCN1A; may regulate SCN1A activity By similarity. Interacts with SCN5A; the interaction is direct and may regulate SNC5A density at membranes and function. Interacts with MAPK8IP2; may regulate the MAPK8IP2 scaffolding activity. Ref.8 Ref.10

Subcellular location

Cell projectionfilopodium. Cell projectiongrowth cone. Cell projectiondendrite. Nucleus Ref.7 Ref.10 Ref.11. Cytoplasm Ref.7 Ref.10 Ref.11. Note: Not secreted. Localizes to the lateral membrane and intercalated disks of myocytes. Ref.7 Ref.10 Ref.11

Isoform 1: Nucleus Ref.7 Ref.10 Ref.11.

Isoform 2: Cytoplasm Ref.7 Ref.10 Ref.11.

Tissue specificity

Detected in brain, eye and heart. In brain, the different isoforms display different patterns of expression. Expressed in brain and heart (at protein level). Isoform 3 is highly expressed in cardiac myocytes while isoform 1 is the most abundant in brain. Ref.2 Ref.7 Ref.10

Developmental stage

Expressed in the subplate of the embryonic cortex and the axonal tracts in the intermediate zone, and in axonal tracts of projection neurons, specifically in the corticothalamic tract and the corpus callosum (at protein level). Isoform 2 is transiently expressed in the neocortex and hippocampus from E17 to P7 (at protein level). In embryonic brain, present in all divisions of the central and peripheral nervous system and it is at least 5 times more abundant than other FHFs. Detected in the subplate, ganglionic eminences, and proliferative zones of the cortical wall at E14. Detected in the cortical plate of the cerebral cortex, hippocampus, and striatum from E17 to P14. Expression is markedly reduced in adult brain where it is most abundant in hippocampus. Also detected in developing kidney. Ref.2

Post-translational modification

May be phosphorylated By similarity.

Disruption phenotype

Conditional knockout mice lacking fgf13 in the cerebral cortex or mice lacking fgf13 in most tissues display similar phenotypes of impaired spatial acquisition and memory. The cued memory and the capacity of novel object recognition are altered. They also display anxiety-related and reduced depression-like behaviors. This is associated with a disorganization of cortical structure and neural circuits. The laminar formation of the neocortex is delayed and the hippocampal development is also affected. Ref.11

Sequence similarities

Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell projection
Cytoplasm
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from electronic annotation. Source: Ensembl

cerebral cortex cell migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

establishment of neuroblast polarity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

hippocampus development

Inferred from mutant phenotype Ref.11. Source: UniProtKB

learning

Inferred from mutant phenotype Ref.11. Source: UniProtKB

memory

Inferred from mutant phenotype Ref.11. Source: UniProtKB

microtubule polymerization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of collateral sprouting

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of microtubule depolymerization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

neuron migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

protein localization to plasma membrane

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

dendrite

Inferred from direct assay Ref.11. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: InterPro

filopodium

Inferred from direct assay Ref.11. Source: UniProtKB

growth cone

Inferred from direct assay Ref.11. Source: UniProtKB

intercalated disc

Inferred from direct assay Ref.10. Source: UniProtKB

microtubule

Inferred from direct assay Ref.11. Source: UniProtKB

neuron projection

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionbeta-tubulin binding

Inferred from direct assay Ref.11. Source: UniProtKB

ion channel binding

Inferred from physical interaction Ref.10. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein kinase activator activity

Inferred from electronic annotation. Source: Ensembl

sodium channel regulator activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P70377-1)

Also known as: FGF13A; mFHF-2(1S); FGF13-S;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P70377-2)

Also known as: FGF13B; mFHF-2(1U); FGF13-U;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLFGSKKRRRRRP → MALLRKSYS
Isoform 3 (identifier: P70377-3)

Also known as: FGF13-VY; mFHF-2(1Y+1V);

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: MAAAIASSLI...SKKRRRRRPE → MSGKVTKPKE...HHKENTEPEE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Fibroblast growth factor 13
PRO_0000147608

Regions

Region1 – 6262Mediates targeting to the nucleus
Region67 – 201135Mediates interaction with sodium channels By similarity
Region157 – 1648Tubulin-binding domain necessary and sufficient for tubulin-binding

Natural variations

Alternative sequence1 – 6363MAAAI…RRRPE → MSGKVTKPKEEKDASKVLDD APPGTQEYIMLRQDSIQSAE LKKKESPFRAKCHEIFCCPP KQVHHKENTEPEE in isoform 3.
VSP_044130
Alternative sequence1 – 6262MAAAI…RRRRP → MALLRKSYS in isoform 2.
VSP_044131

Experimental info

Sequence conflict21A → T in AAB18918. Ref.1
Sequence conflict21Missing in AAB71606. Ref.2
Sequence conflict1991L → Q in AAB71606. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FGF13A) (mFHF-2(1S)) (FGF13-S) [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 5B96D41AC3A3DF78

FASTA24527,588
        10         20         30         40         50         60 
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR 

        70         80         90        100        110        120 
RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK 

       130        140        150        160        170        180 
LYLAMNSEGY LYTSEHFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM 

       190        200        210        220        230        240 
KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS 


HNEST 

« Hide

Isoform 2 (FGF13B) (mFHF-2(1U)) (FGF13-U) [UniParc].

Checksum: 7736A3671677B263
Show »

FASTA19221,605
Isoform 3 (FGF13-VY) (mFHF-2(1Y+1V)) [UniParc].

Checksum: E0EAE1C9DFFBE0EA
Show »

FASTA25528,760

References

« Hide 'large scale' references
[1]"Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development."
Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.
Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Eye.
[2]"Murine FGF-12 and FGF-13: expression in embryonic nervous system, connective tissue and heart."
Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D., Goldfarb M.
Mech. Dev. 64:31-39(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Spinal ganglion.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[7]"Isoform diversity among fibroblast growth factor homologous factors is generated by alternative promoter usage and differential splicing."
Munoz-Sanjuan I., Smallwood P.M., Nathans J.
J. Biol. Chem. 275:2589-2597(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]"Fibroblast growth factor homologous factors are intracellular signaling proteins."
Schoorlemmer J., Goldfarb M.
Curr. Biol. 11:793-797(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAPK SIGNALING, INTERACTION WITH MAPK8IP2.
[9]"Fibroblast growth factor homologous factors and the islet brain-2 scaffold protein regulate activation of a stress-activated protein kinase."
Schoorlemmer J., Goldfarb M.
J. Biol. Chem. 277:49111-49119(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAPK SIGNALING.
[10]"Fibroblast growth factor homologous factor 13 regulates Na+ channels and conduction velocity in murine hearts."
Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V., Puranam R.S., Rosenberg P.B., Bursac N., Pitt G.S.
Circ. Res. 109:775-782(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SODIUM CHANNEL REGULATION, TISSUE SPECIFICITY, INTERACTION WITH SCN5A, SUBCELLULAR LOCATION.
[11]"Fibroblast growth factor 13 is a microtubule-stabilizing protein regulating neuronal polarization and migration."
Wu Q.F., Yang L., Li S., Wang Q., Yuan X.B., Gao X., Bao L., Zhang X.
Cell 149:1549-1564(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURON POLARIZATION, FUNCTION IN NEURON MIGRATION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TUBULIN-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U66202 mRNA. Translation: AAB18918.1.
AF020737 mRNA. Translation: AAB71606.1.
AK141848 mRNA. Translation: BAE24857.1.
AL669891, AL672247, AL713968 Genomic DNA. Translation: CAM19176.1.
AL713968, AL672247 Genomic DNA. Translation: CAM22824.1.
AL713968, AL672247 Genomic DNA. Translation: CAM22825.1.
AL713968, AL669891, AL672247 Genomic DNA. Translation: CAM22827.1.
AL672247, AL713968 Genomic DNA. Translation: CAM27417.1.
AL672247, AL713968 Genomic DNA. Translation: CAM27418.1.
AL672247, AL669891, AL713968 Genomic DNA. Translation: CAM27420.1.
CH466583 Genomic DNA. Translation: EDL42180.1.
CH466583 Genomic DNA. Translation: EDL42182.1.
BC018238 mRNA. Translation: AAH18238.1.
AF199608 mRNA. Translation: AAF31395.1.
RefSeqNP_034330.2. NM_010200.2.
XP_006527861.1. XM_006527798.1.
UniGeneMm.7995.

3D structure databases

ProteinModelPortalP70377.
SMRP70377. Positions 64-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033473.

PTM databases

PhosphoSiteP70377.

Proteomic databases

PaxDbP70377.
PRIDEP70377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033473; ENSMUSP00000033473; ENSMUSG00000031137. [P70377-1]
ENSMUST00000119306; ENSMUSP00000113206; ENSMUSG00000031137. [P70377-2]
GeneID14168.
KEGGmmu:14168.
UCSCuc009tht.2. mouse.
uc009thu.2. mouse.

Organism-specific databases

CTD2258.
MGIMGI:109178. Fgf13.

Phylogenomic databases

eggNOGNOG308177.
GeneTreeENSGT00730000110666.
HOGENOMHOG000290676.
HOVERGENHBG007580.
InParanoidP70377.
KOK04358.
OMAKSNACRC.
OrthoDBEOG7J447D.
TreeFamTF317805.

Gene expression databases

ArrayExpressP70377.
CleanExMM_FGF13.
GenevestigatorP70377.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028279. FGF13.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF16. PTHR11486:SF16. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGF13. mouse.
NextBio285320.
PROP70377.
SOURCESearch...

Entry information

Entry nameFGF13_MOUSE
AccessionPrimary (citable) accession number: P70377
Secondary accession number(s): B1AU21 expand/collapse secondary AC list , O35338, Q3UR31, Q8VCY9, Q9JLA5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot